6JSJ

Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1

6JSJ の概要

• エントリーDOI: 10.2210/pdb6jsj/pdb
• 分子名称: Dynamin-like GTPase MGM1, mitochondrial, GUANOSINE-5'-DIPHOSPHATE, IODIDE ION (3 entities in total)
• 機能のキーワード: mitochondria, fusion, mgm1, hydrolase
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 241703.74

構造登録者

Yan, L.,Li, L. (登録日: 2019-04-08, 公開日: 2020-02-19, 最終更新日: 2024-11-20)

主引用文献

Yan, L.,Qi, Y.,Ricketson, D.,Li, L.,Subramanian, K.,Zhao, J.,Yu, C.,Wu, L.,Sarsam, R.,Wong, M.,Lou, Z.,Rao, Z.,Nunnari, J.,Hu, J.
Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.
Proc.Natl.Acad.Sci.USA, 117:4061-4070, 2020

PubMed Abstract: The fusion of inner mitochondrial membranes requires dynamin-like GTPases, Mgm1 in yeast and OPA1 in mammals, but how they mediate membrane fusion is poorly understood. Here, we determined the crystal structure of short Mgm1 (s-Mgm1) in complex with GDP. It revealed an N-terminal GTPase (G) domain followed by two helix bundles (HB1 and HB2) and a unique C-terminal lipid-interacting stalk (LIS). Dimers can form through antiparallel HB interactions. Head-to-tail trimers are built by intermolecular interactions between the G domain and HB2-LIS. Biochemical and in vivo analyses support the idea that the assembly interfaces observed here are native and critical for Mgm1 function. We also found that s-Mgm1 interacts with negatively charged lipids via both the G domain and LIS. Based on these observations, we propose that membrane targeting via the G domain and LIS facilitates the in cis assembly of Mgm1, potentially generating a highly curved membrane tip to allow inner membrane fusion.

PubMed: 32041880
DOI: 10.1073/pnas.1919116117

実験手法

X-RAY DIFFRACTION (3.2 Å)